| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01019433001 |
| Family | GH5 |
| Protein Properties | Length: 562 Molecular Weight: 63046.2 Isoelectric Point: 9.0128 |
| Chromosome | Chromosome/Scaffold: 2 Start: 662067 End: 666143 |
| Description | Cellulase (glycosyl hydrolase family 5) protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH5 | 53 | 368 | 3e-39 |
| DASGQRVKLACVNWISHLQAMVVEGLHKRPLREIAGGITAMGFNCVRLTWATYMFTRPSYGNRSVAESLGELGLSEAKEGVARNNPELLNLSLVEAYEAV VDELGRHGVMVVLDNHVSKPKWCCAEDDGNGFFGDKYFHPKEWLQGLTKVAHRFKDKSQVVAMSMRNELRGPNQTEHIWYKQIRKGGRTIHSINPNLLVI VSGLEFDTDLSFLKQKPLKLKLPNKVVFEAHWYSFSSITGGVEWTEQPLNQICHNRTEWFESGAAFVGTGSNPAPFFLSEFGIDLRGVNPRDNRFFGCFL AFVAQRDLDWALWTLQ | |||
| Full Sequence |
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| Protein Sequence Length: 562 Download |
| MRGLYSLFAR GPMYIIMKEK RSIATILFIS LLLFASDSHS LPLSTRGRWV VDDASGQRVK 60 LACVNWISHL QAMVVEGLHK RPLREIAGGI TAMGFNCVRL TWATYMFTRP SYGNRSVAES 120 LGELGLSEAK EGVARNNPEL LNLSLVEAYE AVVDELGRHG VMVVLDNHVS KPKWCCAEDD 180 GNGFFGDKYF HPKEWLQGLT KVAHRFKDKS QVVAMSMRNE LRGPNQTEHI WYKQIRKGGR 240 TIHSINPNLL VIVSGLEFDT DLSFLKQKPL KLKLPNKVVF EAHWYSFSSI TGGVEWTEQP 300 LNQICHNRTE WFESGAAFVG TGSNPAPFFL SEFGIDLRGV NPRDNRFFGC FLAFVAQRDL 360 DWALWTLQGS YYYRDGVVGQ EETYGVLDYN WDKPRNPKFL KRIRILQDIL QDPNSNVPKY 420 HLIFHPRSGR CVSVKGEGQD QIHGRNCKKG SRWSHDGNGG AIRLMGSGLC LKAVGDGLPA 480 KLSTDCSSPQ ARWKLISKSK LHIAAMDEQG KPLCLDGKNS NSSSILTRTC ICALQDGDGS 540 DLDCLTNPQR QWFKFVPSNL P* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00458 | RICIN | 0.0003 | 423 | 534 | 119 | + Ricin-type beta-trefoil. Carbohydrate-binding domain formed from presumed gene triplication. | ||
| cd00161 | RICIN | 2.0e-5 | 420 | 530 | 120 | + Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. The domain is found in a variety of molecules serving diverse functions such as enzymatic activity, inhibitory toxicity and signal transduction. Highly specific ligand binding occurs on exposed surfaces of the compact domain sturcture. | ||
| pfam00150 | Cellulase | 7.0e-8 | 90 | 367 | 287 | + Cellulase (glycosyl hydrolase family 5). | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI34404.1 | 0 | 1 | 561 | 1 | 561 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002272386.1 | 0 | 21 | 560 | 4 | 531 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002272422.1 | 0 | 21 | 560 | 87 | 614 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002272491.1 | 0 | 22 | 561 | 8 | 541 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002272534.1 | 0 | 17 | 561 | 1 | 545 | PREDICTED: hypothetical protein [Vitis vinifera] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1vrx_B | 4e-17 | 45 | 366 | 8 | 320 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
| PDB | 1vrx_A | 4e-17 | 45 | 366 | 8 | 320 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
| PDB | 1ece_B | 4e-16 | 45 | 366 | 8 | 320 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
| PDB | 1ece_A | 4e-16 | 45 | 366 | 8 | 320 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
| PDB | 4dm1_C | 0.00000008 | 49 | 285 | 16 | 266 | A Chain A, Contribution Of Disulfide Bond Toward Thermostability In Hyperthermostable Endocellulase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| DY937433 | 309 | 22 | 326 | 0 |
| DY937488 | 294 | 21 | 310 | 0 |
| DY941710 | 294 | 21 | 310 | 0 |
| DY941215 | 298 | 17 | 310 | 0 |
| CV135080 | 310 | 28 | 336 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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